ID Q84FM6_CAMJU Unreviewed; 639 AA.
AC Q84FM6;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Tetracycline resistance protein {ECO:0000313|EMBL:AAO38916.1};
GN Name=tetO {ECO:0000313|EMBL:AAO38916.1};
OS Campylobacter jejuni.
OG Plasmid pCjA13 {ECO:0000313|EMBL:AAO38916.1}.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=197 {ECO:0000313|EMBL:AAO38916.1};
RN [1] {ECO:0000313|EMBL:AAO38916.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pCjA13 {ECO:0000313|EMBL:AAO38916.1};
RX PubMed=15603835; DOI=10.1016/j.jinf.2004.02.013;
RA Schmidt-Ott R., Pohl S., Burghard S., Weig M., Gross U.;
RT "Identification and characterization of a major subgroup of conjugative
RT Campylobacter jejuni plasmids.";
RL J. Infect. 50:12-21(2005).
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DR EMBL; AY190525; AAO38916.1; -; Genomic_DNA.
DR RefSeq; WP_032490535.1; NG_048256.1.
DR AlphaFoldDB; Q84FM6; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03711; Tet_C; 1.
DR CDD; cd03690; Tet_II; 1.
DR CDD; cd16258; Tet_III; 1.
DR CDD; cd01684; Tet_like_IV; 1.
DR CDD; cd04168; TetM_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR035650; Tet_C.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR PRINTS; PR01037; TCRTETOQM.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plasmid {ECO:0000313|EMBL:AAO38916.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 1..244
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 639 AA; 72408 MW; D4FF6A87999DA4F6 CRC64;
MKIINLGILA HVDAGKTTLT ESLLYTSGAI AELGSVDEGT TRTDTMNLER QRGITIQTAV
TSFQWEDVKV NIIDTPGHMD FLAEVYRSLS ALDGAVLLVS AKDGIQAQTR ILFHALQIMK
IPTIFFINKI DQEGIDLPMV YREMKAKLSS EIIVKQKVGQ HPHINVTDND DMEQWDAVIM
GNDELLEKYM SGKPFKMSEL EQEENRRFQN GTLFPVYHGS AKNNLGIRQL IEVIASKFYS
STPEGQSELC GRVFKIEYSK KRRRFVYVRI YSGTLHLRDV IRISEKEKIK ITEMCVPTNG
ELYSSDTACS GDIVILPNDV LQLNSILGNE ILLPQRKFIE NPLPMLQTTI AVKKSEQREI
LLGALTEISD GDPLLKYYVD TTTHEIILSF LGNVQMEVIC AILEEKYHVE AEIKEPTVIY
MERPLRKAEY TIHIEVPPNP FWASVGLSIE PLPIGSGVQY ESRVSLGYLN QSFQNAVMEG
VLYGCEQGLY GWKVTDCKIC FEYGLYYSPV STPADFRLLS PIVLEQALKK AGTELLEPYL
HFEIYAPQEY LSRAYHDAPR YCADIVSTQI KNDEVILKGE IPARCIQEYR NDLTCFTNGQ
GVCLTELKGY QPAIGKFICQ PRRPNSRIDK VRHMFHKLA
//
